thyroid nodule/protease

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Reduced proteolytic activity in vitro of lysosomes isolated from "cold" thyroid nodule.

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The proteolytic activity of lysosomes isolated from solitary "cold" thyroid nodule and morphologically normal perinodular thyroid tissue was examined in parallel in an in vitro system using 125I-labelled rat Tg as substrate. Lysosomes were isolated by centrifugation of the tissue homogenates between

Acid thyroglobulin protease activities in human diseased thyroid glands.

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The lysosomal acid protease is thought to be a main enzyme in hydrolysis of thyroglobulin. The protease activity of lysosome-rich fractions of various diseased thyroid glands were assayed by the sensitive and reproducible method developed in our laboratory. They included 78 diseased thyroid glands;

High-accuracy Detection of Preoperative Thyroid Nodules Using Combination of BRAFV600E Mutation and TMPRSS4 mRNA Level.

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Papillary thyroid cancer (PTC) is the most common epithelial thyroid tumor, accounting for more than 80% of all thyroid cancers. Though the fine needle aspiration biopsy (FNAB) represents as the golden standard for the diagnostics of thyroid nodules, there is a ∼25% risk of

Diagnostic and extent of disease multigene assay for malignant thyroid neoplasms.

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BACKGROUND Approximately 30% of fine-needle aspiration (FNA) biopsies of thyroid nodules are indeterminate, nondiagnostic, or suspicious. The purpose of the current study was to determine the accuracy of novel candidate diagnostic markers to distinguish benign from malignant thyroid neoplasms, and

Vitamin D receptor expression is linked to potential markers of human thyroid papillary carcinoma.

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Genes regulated cell-cell and cell-matrix adhesion and degradation of the extracellular matrix (ECM) have been screened as potential markers of malignant thyroid nodules. The mRNA expression levels of two of them, the ECM protein-1 (ECM1) and the type II transmembrane serine protease-4 (TMPRSS4),

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